Abstract
Many inhibitors of enzymes have been designed by replacing the scissile amide bond in a substrate with a hydrolytically stable functionality, such as hydroxyethylene [1]. The hydroxyethylene (HET) dipeptide isostere serves as a “transition state” inhibitor and mimics the tetrahedral intermediate formed during hydrolysis (Figure 1) [2].
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Singh, S., Baur, P., Pennington, M.W. (2001). Efficient Diastereoselective Synthesis of a Hydroxyethylene Dipeptide Isostere. In: Lebl, M., Houghten, R.A. (eds) Peptides: The Wave of the Future. American Peptide Symposia, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0464-0_13
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DOI: https://doi.org/10.1007/978-94-010-0464-0_13
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